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Fig. 12 | Journal of Genetic Engineering and Biotechnology

Fig. 12

From: Study on cocoonase, sericin, and degumming of silk cocoon: computational and experimental

Fig. 12

a Prediction of conserved domains of cocoonase [Bombyx mori] on [gi|315258604|dbj|BAJ46146.1|] (serine protease with domain architecture ID 10076129) trypsin-like serine protease. Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. However, a few are active as single chain molecules while others are inactive due to substitutions of the catalytic triad residues [47, 48]. Here, pfam00089 [specific hit, evalue = 2.53e−59, trypsin] and COG5640 [non-specific hit, evalue = 9.80e−25, secreted trypsin-like serine protease] were predicted. b Prediction of conserved domains of sericin [Bombyx mori]. No conserved domain was predicted

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